1xky

X-ray diffraction
1.94Å resolution

Crystal Structure of Dihydrodipicolinate Synthase DapA-2 (BA3935) from Bacillus Anthracis at 1.94A Resolution.

Released:

Function and Biology Details

Reaction catalysed:
Pyruvate + L-aspartate-4-semialdehyde = (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate + H(2)O
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-105681 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-hydroxy-tetrahydrodipicolinate synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 301 amino acids
Theoretical weight: 32.32 KDa
Source organism: Bacillus anthracis
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A6L7H340 (Residues: 1-292; Coverage: 100%)
Gene names: GBAA_3935, dapA, dapA2
Sequence domains: Dihydrodipicolinate synthetase family
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 55.203Å b: 126.882Å c: 173.319Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.156 0.153 0.197
Expression system: Escherichia coli